Analytical Data
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Gene name
RSU1
- Application
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Alternative Names
RSP1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15404
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Expression Region
Ser2~Arg277
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Molecular Weight
35kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
RSU1 (Ras superfamily of small GTPases 1) is a protein that plays a critical role in cellular signaling and has been implicated in various biological processes, including cell proliferation, differentiation, and migration. Understanding RSU1's function is vital due to its involvement in several diseases, particularly cancer, where dysregulation of signaling pathways can lead to uncontrolled growth and metastasis. Research has shown that RSU1 interacts with multiple signaling molecules, acting as a regulatory component within the Ras signaling pathway. Additionally, its role in modulating the activity of small GTPases has made it a subject of interest in studying the molecular mechanisms underlying cell behavior and disease pathogenesis. Recent advances in recombinant protein technology have allowed for the production of RSU1 in more significant quantities, facilitating in-depth biochemical and structural analyses. These studies aim to elucidate the structural features of RSU1, its interaction partners, and the downstream effects of its signaling activities, providing potential insights into therapeutic targets for cancer and other diseases associated with RSU1 dysregulation. The ongoing exploration of RSU1 and its associated pathways holds promise for advancing our understanding of fundamental cellular processes and developing novel strategies for intervention in various pathological conditions.
